This is a new core component of the program project 'From Genomic Sequences to Protein Structure and function'. The goal is to determine the solution properties of proteins selected for structural studies. It is expected that many of the human proteins studied in the next phase will require encouragement to fold into their functional conformation, and that a number of the alternatively spliced proteins may not have a folded functional structure. Although it is a small core, it is essential for success, as it will ensure that proper emphasis is placed on determining the solution properties of our proteins. The Pl's extensive experience in studying protein folding, and dealing with solution properties of proteins will be of value throughout the project. A set of standard biophysical techniques wilt be used: (1) Circular dichroism, to obtain an initial indication of the folding state of each protein. (2) One and two-dimensional NMR spectra, to provide precise information of the extent and level of ordering of each protein. (3). MALDI-TOF mass spectroscopy, to provide precise molecular weight and purity information. (4). Dynamic Light Scattering, for initial identification of large aggregates that might interfere with crystallization, and for establishing conditions in which the protein is monodisperse. (5) Size exclusion chromatography, used in addition to Dynamic Light Scattering, to assess the homogeneity, aggregation, and oligomeric state of the sample. (6). Ultracentrifugation, to determine accurately the oligomeric state of each suitable protein. It is expected that in some cases, different alternative splice protein versions will have different oligomeric states.